ID A0A3B7M4Q3_9GAMM Unreviewed; 1155 AA.
AC A0A3B7M4Q3;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Transcription-repair-coupling factor {ECO:0000256|HAMAP-Rule:MF_00969};
DE Short=TRCF {ECO:0000256|HAMAP-Rule:MF_00969};
DE EC=3.6.4.- {ECO:0000256|HAMAP-Rule:MF_00969};
GN Name=mfd {ECO:0000256|HAMAP-Rule:MF_00969};
GN ORFNames=CDG61_09705 {ECO:0000313|EMBL:AXY60272.1};
OS Acinetobacter sp. WCHAc010052.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=2004647 {ECO:0000313|EMBL:AXY60272.1, ECO:0000313|Proteomes:UP000264387};
RN [1] {ECO:0000313|EMBL:AXY60272.1, ECO:0000313|Proteomes:UP000264387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WCHAc010052 {ECO:0000313|EMBL:AXY60272.1,
RC ECO:0000313|Proteomes:UP000264387};
RA Hu Y., Long H., Feng Y., Zong Z.;
RT "The complete genome of Acinetobacter sp. strain WCHAc010052.";
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Couples transcription and DNA repair by recognizing RNA
CC polymerase (RNAP) stalled at DNA lesions. Mediates ATP-dependent
CC release of RNAP and its truncated transcript from the DNA, and
CC recruitment of nucleotide excision repair machinery to the damaged
CC site. {ECO:0000256|HAMAP-Rule:MF_00969}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00969}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the helicase family.
CC RecG subfamily. {ECO:0000256|HAMAP-Rule:MF_00969}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the UvrB family.
CC {ECO:0000256|HAMAP-Rule:MF_00969}.
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DR EMBL; CP032143; AXY60272.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B7M4Q3; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000264387; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:UniProtKB-UniRule.
DR GO; GO:0000716; P:transcription-coupled nucleotide-excision repair, DNA damage recognition; IEA:UniProtKB-UniRule.
DR CDD; cd17991; DEXHc_TRCF; 1.
DR Gene3D; 2.40.10.170; -; 1.
DR Gene3D; 3.40.50.11140; -; 1.
DR Gene3D; 3.40.50.11180; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.30.2060.10; Penicillin-binding protein 1b domain; 1.
DR Gene3D; 3.90.1150.50; Transcription-repair-coupling factor, D7 domain; 1.
DR HAMAP; MF_00969; TRCF; 1.
DR InterPro; IPR003711; CarD-like/TRCF_RID.
DR InterPro; IPR036101; CarD-like/TRCF_RID_sf.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR004576; Mfd.
DR InterPro; IPR048635; MFD_D3.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR047112; RecG/Mfd.
DR InterPro; IPR037235; TRCF-like_C_D7.
DR InterPro; IPR005118; TRCF_C.
DR InterPro; IPR041471; UvrB_inter.
DR NCBIfam; TIGR00580; mfd; 1.
DR PANTHER; PTHR47964; ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC; 1.
DR PANTHER; PTHR47964:SF1; ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC; 1.
DR Pfam; PF02559; CarD_TRCF_RID; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF21132; MFD_D3; 1.
DR Pfam; PF03461; TRCF; 1.
DR Pfam; PF17757; UvrB_inter; 1.
DR SMART; SM01058; CarD_TRCF; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00982; TRCF; 1.
DR SUPFAM; SSF141259; CarD-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR SUPFAM; SSF143517; TRCF domain-like; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00969}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00969};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_00969};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_00969};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00969}; Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00969};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00969}.
FT DOMAIN 620..781
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 803..956
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1155 AA; 130622 MW; AD05BAD02AD44B61 CRC64;
MFTQEISELN LKQLKAGEKR WIGSMLGSSA ALLFKEISEK SSQLFVLVAR NNQHLGQLES
ELEFYGIKPT IFPDWEILPY DRLSPHQDIV SERLSILSNM PQSGILLVSA TTLAQRVAPT
SWVLGEHFDI KIGQTFDLEQ QKLRLIQAGY HLVDTVYDHG EFAVRGSIMD IYASGQDAPI
RIDLFDNEID TLKFFDPETQ RTTTKIESFT VLPAKEFPLK EARSTFRDRY AESFPTANPK
KNPIYQDVME GIASPGLDFY FPLFFSAEAM QTQSSLISYL PGNAVVITDK HLEDGLTSFW
KDVMRRYEDR RHNVDQPLLP PEQIFLQPNQ IFEFLNQFPR IIADTEVVEI RSGALNLSAE
LPPRLAVDPK QEKPFSAVKK YIDDANHPVL LVAESAGRRE TLKDALCPTL GEIPVVSNFA
EFQQSHFSVA ITNAPLDRGL VITDHLSVIS ENQLYEHRVV QRRRKRQHEV SEEFLVRSLT
ELSIGAPVVH IDHGVGRYAG LITLNIDDQD YEFLQLNYAD EAKVYVPVTN LHLISRFSGG
DPDLAPLHKL GTDAWNKAKR KALEQIHDVA AELLHIQARR QAKPGISFEL EQSSYMQFSS
GFAYEETLDQ ANAIEATLYD MQLAKPMDRL VCGDVGFGKT EVAMRAAFVA VQNNKQVAVL
VPTTLLAQQH YESFKDRFAD WPIRIEVLSR FGTSKAHTRT IEDLADGKVD IVIGTHKILQ
ENIQFKNLGL MIVDEEHRFG VRDKERIKAM RADVDMLTLT ATPIPRTLNM AFSGMRDLSI
IATPPARRLA VKTFVNEQTD ETMKEAILRE LLRGGQVYIL HNEVDTIERA AENIRNLVPE
ARVAVAHGQM RERELEQVMQ QFYHKEFNVL VCSTIIETGI DVPNANTIII ERADKLGLAQ
LHQLRGRVGR SHHQAYAYLM VPSIKGLKGD AEKRLDAISR ASTLGAGFML ATEDLEIRGA
GELLGEQQSG SMQAIGYSLY MEMLEKATKA IQNGKTPNFD APLSLTAEIN LHMPALIPDE
YLGDVHQRLM FYKRISNANT QEKLDHIRME LIDRFGVPPV QVKQLFSVHQ IRIIAEKLEI
TKIDLSANGG SIEFSPDTPV QAITIIQMMQ KHPTWFRMEG GQRLRVMVMM EEYEKRIRFI
SDLLNSLVSE SGLKP
//